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- PDB-2xln: Crystal structure of a complex between Actinomadura R39 DD-peptid... -

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Basic information

Entry
Database: PDB / ID: 2xln
TitleCrystal structure of a complex between Actinomadura R39 DD-peptidase and a boronate inhibitor
ComponentsD-ALANYL-D-ALANINE CARBOXYPEPTIDASE,
KeywordsHYDROLASE / PEPTIDOGLYCAN
Function / homology
Function and homology information


serine-type D-Ala-D-Ala carboxypeptidase / serine-type D-Ala-D-Ala carboxypeptidase activity / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / response to antibiotic / proteolysis / extracellular region
Similarity search - Function
D-Ala-D-Ala carboxypeptidase C, peptidase S13 / Peptidase S13, D-Ala-D-Ala carboxypeptidase C / D-Ala-D-Ala carboxypeptidase 3 (S13) family / D-tyrosyl-trna(Tyr) Deacylase; Chain: A; / Beta-lactamase / DD-peptidase/beta-lactamase superfamily / 3-Layer(bba) Sandwich / Beta-lactamase/transpeptidase-like / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
: / Chem-EWA / D-alanyl-D-alanine carboxypeptidase
Similarity search - Component
Biological speciesACTINOMADURA SP (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsSauvage, E. / Herman, R. / Kerff, F. / Rocaboy, M. / Charlier, P.
CitationJournal: Acs Med.Chem.Lett. / Year: 2011
Title: Structure Guided Development of Potent Reversibly Binding Penicillin Binding Protein Inhibitors
Authors: Woon, E.C.Y. / Zervosen, A. / Sauvage, E. / Simmons, K.J. / Ivec, M. / Inglis, S.R. / Fishwick, C.W.G. / Gobec, S. / Charlier, P. / Luxen, A. / Schofield, C.J.
History
DepositionJul 21, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 26, 2011Provider: repository / Type: Initial release
Revision 1.1Jun 6, 2012Group: Database references / Version format compliance
Revision 1.2Jun 18, 2014Group: Database references
Revision 1.3Nov 6, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE,
B: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE,
C: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE,
D: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE,
hetero molecules


Theoretical massNumber of molelcules
Total (without water)203,09827
Polymers200,3354
Non-polymers2,76323
Water14,700816
1
A: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE,
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,7807
Polymers50,0841
Non-polymers6966
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE,
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,8177
Polymers50,0841
Non-polymers7336
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE,
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,7216
Polymers50,0841
Non-polymers6375
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE,
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,7807
Polymers50,0841
Non-polymers6966
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)102.994, 91.258, 106.878
Angle α, β, γ (deg.)90.00, 94.46, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
D-ALANYL-D-ALANINE CARBOXYPEPTIDASE, / DD-CARBOXYPEPTIDASE / DD-PEPTIDASE / PENICILLIN-BINDING PROTEIN / PBP


Mass: 50083.812 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ACTINOMADURA SP (bacteria) / Strain: R39
References: UniProt: P39045, serine-type D-Ala-D-Ala carboxypeptidase
#2: Chemical
ChemComp-EWA / [(1S)-1-{[(2,6-DIMETHOXYPHENYL)CARBONYL]AMINO}ETHYL]BORONIC ACID


Mass: 253.059 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C11H16BNO5
#3: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 17 / Source method: obtained synthetically / Formula: SO4
#4: Chemical ChemComp-CO / COBALT (II) ION


Mass: 58.933 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Co
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 816 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.49 Å3/Da / Density % sol: 50.2 % / Description: NONE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM30A / Wavelength: 0.9796
DetectorType: MARRESEARCH / Date: Jan 25, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9796 Å / Relative weight: 1
ReflectionResolution: 2.4→35.6 Å / Num. obs: 77046 / % possible obs: 99.6 % / Observed criterion σ(I): 0 / Redundancy: 7 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 18.1
Reflection shellResolution: 2.4→2.53 Å / Redundancy: 6.7 % / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 3.6 / % possible all: 99.5

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→33.35 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.906 / SU B: 15.878 / SU ML: 0.203 / Cross valid method: THROUGHOUT / ESU R: 0.448 / ESU R Free: 0.268 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.24719 3878 5 %RANDOM
Rwork0.1914 ---
obs0.19423 73143 99.6 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 24.847 Å2
Baniso -1Baniso -2Baniso -3
1-0.08 Å20 Å2-0.02 Å2
2--0.12 Å20 Å2
3----0.21 Å2
Refinement stepCycle: LAST / Resolution: 2.4→33.35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13394 0 159 816 14369
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.02113774
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.151.97418846
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.851858
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.47225.47574
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.953151920
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.221568
X-RAY DIFFRACTIONr_chiral_restr0.0890.22182
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0210676
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.1830.26420
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.2960.29285
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1260.2921
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2430.2126
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1510.218
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.321.59341
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.57214556
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.9434944
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it1.5334.54290
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.4→2.462 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.301 290 -
Rwork0.23 5365 -
obs--99.37 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
13.10955.4262-1.22239.8553-3.46615.08020.32520.1803-0.1187-0.2535-0.36160.61781.5916-0.38390.03640.3305-0.07550.04330.32940.0170.3175-16.403-21.03933.256
21.0198-0.1037-0.01540.25930.07190.8567-0.0268-0.02220.03920.0510.0422-0.04670.0571-0.0011-0.01540.06890.0153-0.03250.1698-0.0050.15111.7056.73441.164
31.9163-0.85990.24821.10190.5780.6958-0.0183-0.0185-0.1053-0.0571-0.10560.1123-0.01040.00120.12390.0611-0.0109-0.03450.1510.00650.1782-2.19520.24741.404
42.40080.7663-0.08820.7740.27661.2174-0.0376-0.04830.06480.10670.053-0.1759-0.05720.2158-0.01530.03560.0756-0.04840.15080.00780.13419.8558.90445.238
51.66670.2839-0.34810.7553-0.30771.6465-0.04680.0338-0.19840.10880.0480.02080.2143-0.084-0.00120.06550.0199-0.00720.1035-0.00430.11994.701-10.8237.747
60.91921.3158-1.3282.213-1.05547.6105-0.1979-0.0648-0.30.25690.21620.00920.8729-0.7007-0.01820.0884-0.04290.03510.18940.06080.1847-10.125-18.05642.059
74.89771.43260.22542.897-0.42993.136-0.20910.33280.5413-0.38470.08760.2513-0.8268-0.24090.12150.29670.0876-0.0676-0.07680.08090.093954.44338.65918.653
80.3973-0.10710.16111.0137-0.33642.3795-0.0166-0.13620.01960.18090.02950.0082-0.062-0.0788-0.01280.0646-0.0201-0.020.1247-0.0220.130159.95515.50254.741
91.326-0.2577-1.45740.17150.57752.3149-0.0638-0.2265-0.04040.04450.0343-0.04130.1830.37590.02950.05210.0087-0.03910.13870.0280.119376.5728.69243.307
100.6189-0.09590.23251.0573-0.66292.67340.0235-0.11510.05890.12350.04730.0639-0.1314-0.2289-0.07090.0839-0.00430.00110.0805-0.0330.130555.02420.06949.2
111.50580.3841-0.57321.0362-1.44282.22750.0641-0.11920.1530.1643-0.0327-0.0203-0.56820.0899-0.03140.23150.00380.0046-0.0324-0.00810.146362.2536.04634.996
124.82641.85780.34036.79360.73642.935-0.02580.0050.4823-0.28690.09640.0075-0.64520.3214-0.07060.2629-0.01410.0006-0.03270.03970.128162.00439.54224.795
138.01743.56033.68816.7396-1.729811.41760.7398-0.6871.8648-0.5631-0.44930.0042-2.0733-0.6127-0.29050.28080.07530.05690.29040.00980.291513.20793.735-30.569
140.8822-0.1670.10161.2885-0.56311.24930.0298-0.1574-0.01940.16630.0610.1347-0.0338-0.1425-0.09080.07590.00690.03280.1671-0.03720.124213.05363.129-3.423
152.1679-0.6165-1.850.32830.72042.1598-0.06-0.2329-0.13950.05170.0285-0.05680.07530.1490.03160.09850.0017-0.03260.0550.01930.12829.7651.405-10.71
160.94330.0658-0.00680.7497-0.6211.3080.0235-0.13970.08570.19770.02990.125-0.1201-0.1764-0.05340.12320.03720.02810.1142-0.04820.113510.61566.247-2.338
170.4781.1492-0.06873.99830.06530.4807-0.09550.0628-0.00720.24780.0336-0.2729-0.2963-0.07940.06190.16670.0499-0.01610.0714-0.02370.13225.52681.057-14.326
182.8530.34440.54574.48741.87783.1828-0.0051-0.01280.2066-0.11950.085-0.0592-0.351-0.0822-0.080.10560.05740.010.0544-0.0020.133717.50683.653-21.722
198.99870.1958-1.1816.20850.97034.2641-0.2237-0.2443-0.90590.2539-0.052-0.93290.78870.53870.27570.01420.12560.1383-0.08690.29950.398359.66266.84425.796
201.5337-0.46270.05462.3448-0.73951.9369-0.07110.1410.0134-0.45790.18330.3267-0.0215-0.5503-0.11220.1522-0.0867-0.02970.1279-0.00680.110625.0992.2298.669
211.69040.8227-0.27911.4-1.15051.076-0.14420.14940.0679-0.2183-0.0096-0.1720.0124-0.04590.15380.1418-0.02370.02750.0302-0.02120.153345.146103.3910.278
222.9852-1.36270.87663.7846-0.82633.1791-0.16780.25730.1053-0.49540.18460.3599-0.1172-0.7324-0.01680.0603-0.1467-0.10250.20510.04010.018221.27895.3465.545
231.7558-0.1563-0.14381.5936-0.30431.4598-0.1877-0.0339-0.3956-0.36110.0137-0.24770.286-0.04010.1740.1262-0.05250.1177-0.0289-0.01860.20944.17576.24817.75
242.7835-1.4862-0.36328.34863.99476.4621-0.31550.0632-0.7144-0.73720.0434-0.30430.14020.87680.27220.07240.04880.1689-0.06780.08750.462861.72471.61315.665
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 24
2X-RAY DIFFRACTION2A25 - 194
3X-RAY DIFFRACTION3A195 - 249
4X-RAY DIFFRACTION4A250 - 305
5X-RAY DIFFRACTION5A306 - 423
6X-RAY DIFFRACTION6A424 - 466
7X-RAY DIFFRACTION7B1 - 44
8X-RAY DIFFRACTION8B45 - 149
9X-RAY DIFFRACTION9B150 - 250
10X-RAY DIFFRACTION10B251 - 359
11X-RAY DIFFRACTION11B360 - 423
12X-RAY DIFFRACTION12B424 - 465
13X-RAY DIFFRACTION13C1 - 12
14X-RAY DIFFRACTION14C13 - 145
15X-RAY DIFFRACTION15C146 - 247
16X-RAY DIFFRACTION16C248 - 385
17X-RAY DIFFRACTION17C386 - 411
18X-RAY DIFFRACTION18C412 - 465
19X-RAY DIFFRACTION19D1 - 44
20X-RAY DIFFRACTION20D45 - 132
21X-RAY DIFFRACTION21D133 - 251
22X-RAY DIFFRACTION22D252 - 291
23X-RAY DIFFRACTION23D292 - 437
24X-RAY DIFFRACTION24D438 - 466

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